PER1_ARAHY
ID PER1_ARAHY Reviewed; 316 AA.
AC P22195;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cationic peroxidase 1;
DE EC=1.11.1.7;
DE AltName: Full=PNPC1;
DE Flags: Precursor;
GN Name=PNC1;
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2247460; DOI=10.1073/pnas.87.22.8874;
RA Buffard D., Breda C., van Huystee R.B., Asemota O., Pierre M.,
RA Dang Ha D.B., Esnault R.;
RT "Molecular cloning of complementary DNAs encoding two cationic peroxidases
RT from cultivated peanut cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8874-8878(1990).
RN [2]
RP SEQUENCE REVISION TO 47.
RA Esnault R.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND PYROGLUTAMATE FORMATION AT
RP GLN-23.
RX PubMed=8805539; DOI=10.1016/s0969-2126(96)00035-4;
RA Schuller D.J., Ban N., van Huystee R.B., McPherson A., Poulos T.L.;
RT "The crystal structure of peanut peroxidase.";
RL Structure 4:311-321(1996).
CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC biosynthesis and degradation of lignin, suberization, auxin catabolism,
CC response to environmental stresses such as wounding, pathogen attack
CC and oxidative stress. These functions might be dependent on each
CC isozyme/isoform in each plant tissue.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR EMBL; M37636; AAB06183.1; -; mRNA.
DR PIR; A38265; A38265.
DR PDB; 1SCH; X-ray; 2.56 A; A/B=24-316.
DR PDBsum; 1SCH; -.
DR AlphaFoldDB; P22195; -.
DR SMR; P22195; -.
DR PeroxiBase; 102; AhPrx04.
DR GlyConnect; 78; 2 N-Linked glycans (1 site).
DR EvolutionaryTrace; P22195; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00693; secretory_peroxidase; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31388; PTHR31388; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..316
FT /note="Cationic peroxidase 1"
FT /id="PRO_0000023746"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 191
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT SITE 60
FT /note="Transition state stabilizer"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:8805539"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000185"
FT DISULFID 33..113
FT DISULFID 66..71
FT DISULFID 119..312
FT DISULFID 198..223
FT TURN 26..32
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:1SCH"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1SCH"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1SCH"
FT TURN 90..95
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 99..112
FT /evidence="ECO:0007829|PDB:1SCH"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:1SCH"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:1SCH"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:1SCH"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:1SCH"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1SCH"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1SCH"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:1SCH"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:1SCH"
FT HELIX 281..295
FT /evidence="ECO:0007829|PDB:1SCH"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1SCH"
SQ SEQUENCE 316 AA; 33518 MW; 2CC271F8E8B8C9F0 CRC64;
MALPISKVDF LIFMCLIGLG SAQLSSNFYA TKCPNALSTI KSAVNSAVAK EARMGASLLR
LHFHDCFVQG CDASVLLDDT SNFTGEKTAG PNANSIRGFE VIDTIKSQVE SLCPGVVSCA
DILAVAARDS VVALGGASWN VLLGRRDSTT ASLSSANSDL PAPFFNLSGL ISAFSNKGFT
TKELVTLSGA HTIGQAQCTA FRTRIYNESN IDPTYAKSLQ ANCPSVGGDT NLSPFDVTTP
NKFDNAYYIN LRNKKGLLHS DQQLFNGVST DSQVTAYSNN AATFNTDFGN AMIKMGNLSP
LTGTSGQIRT NCRKTN
